Evidence map›Paper›PMID 35522180›Full record

ArticleThe Journal of cell biology2022

Signaling by the integrated stress response kinase PKR is fine-tuned by dynamic clustering.

Francesca Zappa, Nerea L Muniozguren, Maxwell Z Wilson, Michael S Costello, Jose Carlos Ponce-Rojas, Diego Acosta-Alvear

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.4field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

28 citing papers in PubMed, 46 citations in OpenAlex.

  1. Structural insights into HRI kinase activity and inhibition.Biochemical Society transactions · 2026
    Review
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  5. Review
  6. Article
  7. Review
  8. Mitochondria-Nuclear Crosstalk: Orchestrating mtDNA Maintenance.Environmental and molecular mutagenesis · 2025
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. A closer look at mammalian antiviral condensates.Biochemical Society transactions · 2024
    Review
  14. Article
  15. Crosstalk between vault RNAs and innate immunity.Molecular biology reports · 2024
    Review
  16. Article
  17. Review
  18. Understanding the impact ofFrontiers in molecular biosciences · 2024
    Review
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Francesca ZappaDepartment of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, Santa Barbara, CA.ORCID 0000-0003-1263-3828
Nerea L MuniozgurenDepartment of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, Santa Barbara, CA.
Maxwell Z WilsonDepartment of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, Santa Barbara, CA.ORCID 0000-0003-0768-7004
Michael S CostelloDepartment of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, Santa Barbara, CA.ORCID 0000-0003-4132-6966
Jose Carlos Ponce-RojasDepartment of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, Santa Barbara, CA.ORCID 0000-0002-0925-3990
Diego Acosta-AlvearDepartment of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, Santa Barbara, CA.ORCID 0000-0002-1139-8486
University of California, Santa Barbara · US

Funding

Calico Life Sciences LLCOtis Williams Postdoctoral FellowshipUCSB Academic Senate Faculty Research
6 · The paper itself

Abstract

The double-stranded RNA sensor kinase PKR is one of four integrated stress response (ISR) sensor kinases that phosphorylate the α subunit of eukaryotic initiation factor 2 (eIF2α) in response to stress. The current model of PKR activation considers the formation of back-to-back PKR dimers as a prerequisite for signal propagation. Here we show that PKR signaling involves the assembly of dynamic PKR clusters. PKR clustering is driven by ligand binding to PKR's sensor domain and by front-to-front interfaces between PKR's kinase domains. PKR clusters are discrete, heterogeneous, autonomous coalescences that share some protein components with processing bodies. Strikingly, eIF2α is not recruited to PKR clusters, and PKR cluster disruption enhances eIF2α phosphorylation. Together, these results support a model in which PKR clustering may limit encounters between PKR and eIF2α to buffer downstream signaling and prevent the ISR from misfiring.

Indexed as

eIF-2 KinaseEukaryotic Initiation Factor-2PhosphorylationRNA, Double-StrandedeIF-2 KinaseEukaryotic Initiation Factor-2RNA, Double-Stranded

Identifiers

PMID35522180
PMCPMC9086502
OpenAlexW4229016690

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.